Inactivation studies of the leucocyte inhibitor of urokinase by cathepsin D.
Leucocytes contain an urokinase inhibitor, that can be inactivated by cathepsin D. In this work biochemical and immunological studies on the inactivation of this inhibitor by cathepsin D are presented. Examinations by polyacrylamide gel electrophoresis and SDS electrophoresis indicate that cathepsin D inactivates urokinase inhibitor by hydrolysis of the inhibitor molecule and that the degradation needed for total inactivation is different from that for formation of the precipitin line with antibodies. The conversion of active inhibitor into inactive protein proceeds catalytically.
D000818:Animals; D001798:Blood Proteins / Q000037:antagonists & inhibitors*; D002402:Cathepsin D; D002403:Cathepsins / Q000494:pharmacology*; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D008970:Molecular Weight; D010446:Peptide Fragments; D013552:Swine
D001798:Blood Proteins; D010446:Peptide Fragments; C031220:urokinase inhibitor; D002403:Cathepsins; D002402:Cathepsin D